Evidence map›Paper›PMID 34638920›Full record

ReviewInternational journal of molecular sciences2021

Glycan-Lectin Interactions in Cancer and Viral Infections and How to Disrupt Them.

Stefanie Maria Kremsreiter, Ann-Sophie Helene Kroell, Katharina Weinberger, Heike Boehm

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.0field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Chimerolectins: Classification, structural architecture, and functional perspectives.Protein science : a publication of the Protein Society · 2025
    Review
  5. Review
  6. Review
  7. Review
  8. A Critical Role of DC-SIGNImmunoTargets and therapy · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Lectin Receptors in Primary and Metastatic Cancer Cells.Asian Pacific journal of cancer prevention : APJCP · 2024
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Stefanie Maria KremsreiterInstitute for Pharmacy and Molecular Biotechnology (IPMB), Ruprecht Karls University Heidelberg, Im Neuenheimer Feld 364, 69120 Heidelberg, Germany.ORCID 0000-0001-8651-3656
Ann-Sophie Helene KroellInstitute for Pharmacy and Molecular Biotechnology (IPMB), Ruprecht Karls University Heidelberg, Im Neuenheimer Feld 364, 69120 Heidelberg, Germany.ORCID 0000-0001-9986-0737
Katharina WeinbergerInstitute for Pharmacy and Molecular Biotechnology (IPMB), Ruprecht Karls University Heidelberg, Im Neuenheimer Feld 364, 69120 Heidelberg, Germany.ORCID 0000-0002-8805-5094
Heike BoehmMax-Planck-Institute for Medical Research, Jahnstr. 29, 69120 Heidelberg, Germany.ORCID 0000-0002-7124-4913
Heidelberg University · DEMax Planck Institute for Medical Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycan-lectin interactions play an essential role in different cellular processes. One of their main functions is involvement in the immune response to pathogens or inflammation. However, cancer cells and viruses have adapted to avail themselves of these interactions. By displaying specific glycosylation structures, they are able to bind to lectins, thus promoting pathogenesis. While glycan-lectin interactions promote tumor progression, metastasis, and/or chemoresistance in cancer, in viral infections they are important for viral entry, release, and/or immune escape. For several years now, a growing number of investigations have been devoted to clarifying the role of glycan-lectin interactions in cancer and viral infections. Various overviews have already summarized and highlighted their findings. In this review, we consider the interactions of the lectins MGL, DC-SIGN, selectins, and galectins in both cancer and viral infections together. A possible transfer of ways to target and disrupt them might lead to new therapeutic approaches in different pathological backgrounds.

Indexed as

AnimalsCell Adhesion MoleculesDC-Specific ICAM-3 Grabbing NonintegrinGalectinsHumansLectinsLectins, C-TypeNeoplasmsPolysaccharidesProtein BindingReceptors, Cell SurfaceSelectinsVirus DiseasesCell Adhesion MoleculesDC-Specific ICAM-3 Grabbing NonintegrinGalectinsLectinsLectins, C-TypePolysaccharidesReceptors, Cell SurfaceSelectinscancerDC-SIGNgalectinsglycosylationlectinsMGLselectinsvirus

Identifiers

PMID34638920
PMCPMC8508825
OpenAlexW3204792239

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.